Chk2 kinase is required for methylglyoxal‐induced G<sub>2</sub>/M cell‐cycle checkpoint arrest: implication of cell‐cycle checkpoint regulation in diabetic oxidative stress signaling

Kani, Shuichi; Nakayama, Emiko; Yoda, Akinori; Onishi, Nobuyuki; Sougawa, Nagako; Hazaka, Yuki; Umeda, Tomohiro; Takeda, Kohsuke; Ichijo, Hidenori; Hamada, Y.; Minami, Yasuhiro

doi:10.1111/j.1365-2443.2007.01100.x

Cited by 22 publications

(16 citation statements)

References 48 publications

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“…The efficiency of the aphidicolin and nocodazole treatments was determined by examining the percentage of cells undergoing mitosis by immunofluorescence analysis of DAPI-stained cells. In agreement with published results, we found that the number of HEK-T, HEK-TPKD and HEK-TPKD3 cells undergoing mitosis reached a peak (20–30%) between 12–14 h after aphidicolin removal [22,23] and 50–70% 12 h after nocodazole incubation [26–28]. IEC-18 cells were synchronized at G 1 /S using the procedure described above for HEK-293 cells.…”

Section: Methodssupporting

confidence: 90%

“…After aspirating the final wash, the cells were incubated in fresh medium with 10% FBS, supplemented or not, with 100 ng/ml Tet plus aphidicolin and cell lysates obtained at the indicated times by lysing the monolayers in 2× SDS-protein sample buffer. A synchronization protocol previously described [20] was used to obtain G 2 /M HEK-293 derived cultures [26–28]. Briefly, cells plated in 60-mm dishes at 1.5×10 5 cells/dish in complete medium were incubated for 18–20 h at 37 °C before being rinsed 3× with DMEM and incubated in DMEM supplemented with 0.2% FBS, plus or minus Tet (100 ng/ml), for 36 h at 37 °C.…”

Section: Methodsmentioning

confidence: 99%

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Protein kinase D isozymes activation and localization during mitosis

Papazyan

Doche

Waldron

et al. 2008

Experimental Cell Research

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The protein kinase D (PKD) family consists of three serine/threonine protein kinases involved in the regulation of fundamental biological processes in response to their activation and intracellular redistribution. Although a substantial amount of information is available describing the mechanisms regulating the activation and intracellular distribution of the PKD isozymes during interphase, nothing is known of their activation status, localization and role during mitosis. The results presented in this study indicate that during mitosis, PKD3 and PKD are phosphorylated at Ser731 and Ser744 within their activation loop by a mechanism that requires protein kinase C. Mitosis-associated PKD3 Ser731 and PKD Ser744 phosphorylation is related to the catalytic activation of these kinases as evidenced by in vivo phosphorylation of histone deacetylase 5, a substrate of PKD and PKD3. Activation loop-phosphorylated PKD3 and PKD, as well as PKD2, associate with centrosomes, spindles and midbody suggesting that these activated kinases establish dynamic interactions with the mitotic apparatus. Thus, this study reveals a connection between the PKD isozymes and cell division, suggesting a novel role for this family of serine/threonine kinases.

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Section: Methodssupporting

confidence: 90%

Section: Methodsmentioning

confidence: 99%

Protein kinase D isozymes activation and localization during mitosis

Papazyan

Doche

Waldron

et al. 2008

Experimental Cell Research

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“…On the other hand, ATM was shown to be downstream of platelet-derived growth factor beta (PDGF beta) receptor activation by hydrogen peroxide, which leads to the phosphorylation and activation of the p53 [63]. In mammalian cells, oxidative stress also leads to the activation of MAP kinases, p38 MAPK and JNK pathways, which might contribute to the activation of ATM through crosstalk between these pathways [64,65].…”

Section: Atm Deficiency and Oxidative Stressmentioning

confidence: 99%

ATM Activation by Oxidative Stress

Guo

Kozlov

Lavin

et al. 2010

Science

955

956

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Stress, DNA Damage, and ATM The protein kinase ATM (ataxia-telangiectasia mutated) is a key component of the signaling pathway through which cells are protected from DNA damage. ATM becomes activated within a protein complex at sites of double-stranded breaks in DNA. ATM is also activated in response to increased production of reactive oxygen species (ROS). Such activation was thought to reflect DNA damage caused by ROS, but Guo et al. (p. 517 ) showed that ATM was in fact directly activated by ROS. A cysteine residue in ATM contributes to the formation of disulfide-linked dimers of activated ATM on exposure to ROS in vitro. Experiments using mutated forms of the enzyme suggested that two distinct mechanisms regulated ATM activity.

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“…The deleterious effect of MG on different types of cells has been extensively studied [30], [31], [32]. A previous study reported an increased apoptotic cell number when mouse Schwann cells were treated with 500–1000 µM MG [31].…”

Section: Discussionmentioning

confidence: 99%

“…An inhibitory effect of MG on cell growth by inducing apoptosis was studied [30], [31], [32]. It is reported that MG promoted programmed cell death through several signaling pathways including growth factor receptor and the gp130/STAT3-signaling pathway.…”

Section: Introductionmentioning

confidence: 99%

Methylglyoxal Mediates Adipocyte Proliferation by Increasing Phosphorylation of Akt1

et al. 2012

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Methylglyoxal (MG) is a highly reactive metabolite physiologically presented in all biological systems. The effects of MG on diabetes and hypertension have been long recognized. In the present study, we investigated the potential role of MG in obesity, one of the most important factors to cause metabolic syndrome. An increased MG accumulation was observed in the adipose tissue of obese Zucker rats. Cell proliferation assay showed that 5–20 µM of MG stimulated the proliferation of 3T3-L1 cells. Further study suggested that accumulated-MG stimulated the phosphorylation of Akt1 and its targets including p21 and p27. The activated Akt1 then increased the activity of CDK2 and accelerated the cell cycle progression of 3T3-L1 cells. The effects of MG were efficiently reversed by advanced glycation end product (AGE) breaker alagebrium and Akt inhibitor SH-6. In summary, our study revealed a previously unrecognized effect of MG in stimulating adipogenesis by up-regulation of Akt signaling pathway and this mechanism might offer a new approach to explain the development of obesity.

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Chk2 kinase is required for methylglyoxal‐induced G₂/M cell‐cycle checkpoint arrest: implication of cell‐cycle checkpoint regulation in diabetic oxidative stress signaling

Abstract: Methylglyoxal (MG) is a reactive endogenous metabolite that is

Cited by 22 publications

References 48 publications

Protein kinase D isozymes activation and localization during mitosis

Protein kinase D isozymes activation and localization during mitosis

ATM Activation by Oxidative Stress

Methylglyoxal Mediates Adipocyte Proliferation by Increasing Phosphorylation of Akt1

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Chk2 kinase is required for methylglyoxal‐induced G2/M cell‐cycle checkpoint arrest: implication of cell‐cycle checkpoint regulation in diabetic oxidative stress signaling

Abstract: Methylglyoxal (MG) is a reactive endogenous metabolite that is

Cited by 22 publications

References 48 publications

Protein kinase D isozymes activation and localization during mitosis

Protein kinase D isozymes activation and localization during mitosis

ATM Activation by Oxidative Stress

Methylglyoxal Mediates Adipocyte Proliferation by Increasing Phosphorylation of Akt1

Contact Info

Product

Resources

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Chk2 kinase is required for methylglyoxal‐induced G₂/M cell‐cycle checkpoint arrest: implication of cell‐cycle checkpoint regulation in diabetic oxidative stress signaling